HIV-1 proteases from drug-naive West African patients are differentially less susceptible to protease inhibitors.
Identifieur interne : 000481 ( PubMed/Curation ); précédent : 000480; suivant : 000482HIV-1 proteases from drug-naive West African patients are differentially less susceptible to protease inhibitors.
Auteurs : Masanobu Kinomoto [Japon] ; Regina Appiah-Opong ; J A M. Brandful ; Masaru Yokoyama ; Nicholas Nii-Trebi ; Evelyn Ugly-Kwame ; Hironori Sato ; David Ofori-Adjei ; Takeshi Kurata ; Françoise Barre-Sinoussi ; Tetsutaro Sata ; Kenzo TokunagaSource :
- Clinical infectious diseases : an official publication of the Infectious Diseases Society of America [ 1537-6591 ] ; 2005.
Descripteurs français
- KwdFr :
- Adulte, Alignement de séquences, Conformation des protéines, Données de séquences moléculaires, Ghana (épidémiologie), Humains, Infections à VIH (virologie), Inhibiteurs de protéase du VIH (pharmacologie), Multirésistance virale aux médicaments, Phylogénie, Protéase du VIH (), Protéase du VIH (métabolisme), Séquence d'acides aminés, VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (enzymologie), VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (génétique).
- MESH :
- enzymologie : VIH-1 (Virus de l'Immunodéficience Humaine de type 1).
- génétique : VIH-1 (Virus de l'Immunodéficience Humaine de type 1).
- métabolisme : Protéase du VIH.
- pharmacologie : Inhibiteurs de protéase du VIH.
- virologie : Infections à VIH.
- épidémiologie : Ghana.
- Adulte, Alignement de séquences, Conformation des protéines, Données de séquences moléculaires, Humains, Multirésistance virale aux médicaments, Phylogénie, Protéase du VIH, Séquence d'acides aminés.
- Wicri :
- geographic : Ghana.
English descriptors
- KwdEn :
- Adult, Amino Acid Sequence, Drug Resistance, Multiple, Viral, Ghana (epidemiology), HIV Infections (virology), HIV Protease (chemistry), HIV Protease (metabolism), HIV Protease Inhibitors (pharmacology), HIV-1 (enzymology), HIV-1 (genetics), Humans, Molecular Sequence Data, Phylogeny, Protein Conformation, Sequence Alignment.
- MESH :
- chemical , chemistry : HIV Protease.
- geographic , epidemiology : Ghana.
- chemical , metabolism : HIV Protease.
- chemical , pharmacology : HIV Protease Inhibitors.
- enzymology : HIV-1.
- genetics : HIV-1.
- virology : HIV Infections.
- Adult, Amino Acid Sequence, Drug Resistance, Multiple, Viral, Humans, Molecular Sequence Data, Phylogeny, Protein Conformation, Sequence Alignment.
Abstract
Now that highly active antiretroviral therapy (HAART) is being initiated on a large scale in West Africa, it remains controversial whether protease inhibitors (PIs), originally designed and tested against human immunodeficiency virus type 1 (HIV-1) subtype B, are equally effective against the non-B subtypes that are prevalent in West African countries. In this study, we investigated whether Ghanaian HIV-1 isolates, as representatives of West African isolates, are susceptible to PIs.
DOI: 10.1086/431197
PubMed: 15983923
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Brandful</name></author><author><name sortKey="Yokoyama, Masaru" sort="Yokoyama, Masaru" uniqKey="Yokoyama M" first="Masaru" last="Yokoyama">Masaru Yokoyama</name></author><author><name sortKey="Nii Trebi, Nicholas" sort="Nii Trebi, Nicholas" uniqKey="Nii Trebi N" first="Nicholas" last="Nii-Trebi">Nicholas Nii-Trebi</name></author><author><name sortKey="Ugly Kwame, Evelyn" sort="Ugly Kwame, Evelyn" uniqKey="Ugly Kwame E" first="Evelyn" last="Ugly-Kwame">Evelyn Ugly-Kwame</name></author><author><name sortKey="Sato, Hironori" sort="Sato, Hironori" uniqKey="Sato H" first="Hironori" last="Sato">Hironori Sato</name></author><author><name sortKey="Ofori Adjei, David" sort="Ofori Adjei, David" uniqKey="Ofori Adjei D" first="David" last="Ofori-Adjei">David Ofori-Adjei</name></author><author><name sortKey="Kurata, Takeshi" sort="Kurata, Takeshi" uniqKey="Kurata T" first="Takeshi" last="Kurata">Takeshi Kurata</name></author><author><name sortKey="Barre Sinoussi, Francoise" sort="Barre Sinoussi, Francoise" uniqKey="Barre Sinoussi F" first="Françoise" last="Barre-Sinoussi">Françoise Barre-Sinoussi</name></author><author><name sortKey="Sata, Tetsutaro" sort="Sata, Tetsutaro" uniqKey="Sata T" first="Tetsutaro" last="Sata">Tetsutaro Sata</name></author><author><name sortKey="Tokunaga, Kenzo" sort="Tokunaga, Kenzo" uniqKey="Tokunaga K" first="Kenzo" last="Tokunaga">Kenzo Tokunaga</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:15983923</idno><idno type="pmid">15983923</idno><idno type="doi">10.1086/431197</idno><idno type="wicri:Area/PubMed/Corpus">000481</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000481</idno><idno type="wicri:Area/PubMed/Curation">000481</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000481</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">HIV-1 proteases from drug-naive West African patients are differentially less susceptible to protease inhibitors.</title><author><name sortKey="Kinomoto, Masanobu" sort="Kinomoto, Masanobu" uniqKey="Kinomoto M" first="Masanobu" last="Kinomoto">Masanobu Kinomoto</name><affiliation wicri:level="1"><nlm:affiliation>Department of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Pathology, National Institute of Infectious Diseases, Tokyo</wicri:regionArea></affiliation></author><author><name sortKey="Appiah Opong, Regina" sort="Appiah Opong, Regina" uniqKey="Appiah Opong R" first="Regina" last="Appiah-Opong">Regina Appiah-Opong</name></author><author><name sortKey="Brandful, J A M" sort="Brandful, J A M" uniqKey="Brandful J" first="J A M" last="Brandful">J A M. Brandful</name></author><author><name sortKey="Yokoyama, Masaru" sort="Yokoyama, Masaru" uniqKey="Yokoyama M" first="Masaru" last="Yokoyama">Masaru Yokoyama</name></author><author><name sortKey="Nii Trebi, Nicholas" sort="Nii Trebi, Nicholas" uniqKey="Nii Trebi N" first="Nicholas" last="Nii-Trebi">Nicholas Nii-Trebi</name></author><author><name sortKey="Ugly Kwame, Evelyn" sort="Ugly Kwame, Evelyn" uniqKey="Ugly Kwame E" first="Evelyn" last="Ugly-Kwame">Evelyn Ugly-Kwame</name></author><author><name sortKey="Sato, Hironori" sort="Sato, Hironori" uniqKey="Sato H" first="Hironori" last="Sato">Hironori Sato</name></author><author><name sortKey="Ofori Adjei, David" sort="Ofori Adjei, David" uniqKey="Ofori Adjei D" first="David" last="Ofori-Adjei">David Ofori-Adjei</name></author><author><name sortKey="Kurata, Takeshi" sort="Kurata, Takeshi" uniqKey="Kurata T" first="Takeshi" last="Kurata">Takeshi Kurata</name></author><author><name sortKey="Barre Sinoussi, Francoise" sort="Barre Sinoussi, Francoise" uniqKey="Barre Sinoussi F" first="Françoise" last="Barre-Sinoussi">Françoise Barre-Sinoussi</name></author><author><name sortKey="Sata, Tetsutaro" sort="Sata, Tetsutaro" uniqKey="Sata T" first="Tetsutaro" last="Sata">Tetsutaro Sata</name></author><author><name sortKey="Tokunaga, Kenzo" sort="Tokunaga, Kenzo" uniqKey="Tokunaga K" first="Kenzo" last="Tokunaga">Kenzo Tokunaga</name></author></analytic><series><title level="j">Clinical infectious diseases : an official publication of the Infectious Diseases Society of America</title><idno type="eISSN">1537-6591</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adult</term><term>Amino Acid Sequence</term><term>Drug Resistance, Multiple, Viral</term><term>Ghana (epidemiology)</term><term>HIV Infections (virology)</term><term>HIV Protease (chemistry)</term><term>HIV Protease (metabolism)</term><term>HIV Protease Inhibitors (pharmacology)</term><term>HIV-1 (enzymology)</term><term>HIV-1 (genetics)</term><term>Humans</term><term>Molecular Sequence Data</term><term>Phylogeny</term><term>Protein Conformation</term><term>Sequence Alignment</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adulte</term><term>Alignement de séquences</term><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Ghana (épidémiologie)</term><term>Humains</term><term>Infections à VIH (virologie)</term><term>Inhibiteurs de protéase du VIH (pharmacologie)</term><term>Multirésistance virale aux médicaments</term><term>Phylogénie</term><term>Protéase du VIH ()</term><term>Protéase du VIH (métabolisme)</term><term>Séquence d'acides aminés</term><term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (enzymologie)</term><term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>HIV Protease</term></keywords><keywords scheme="MESH" type="geographic" qualifier="epidemiology" xml:lang="en"><term>Ghana</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>HIV Protease</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>HIV Protease Inhibitors</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1)</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>HIV-1</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>HIV-1</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1)</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéase du VIH</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Inhibiteurs de protéase du VIH</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Infections à VIH</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>HIV Infections</term></keywords><keywords scheme="MESH" qualifier="épidémiologie" xml:lang="fr"><term>Ghana</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Adult</term><term>Amino Acid Sequence</term><term>Drug Resistance, Multiple, Viral</term><term>Humans</term><term>Molecular Sequence Data</term><term>Phylogeny</term><term>Protein Conformation</term><term>Sequence Alignment</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Adulte</term><term>Alignement de séquences</term><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Multirésistance virale aux médicaments</term><term>Phylogénie</term><term>Protéase du VIH</term><term>Séquence d'acides aminés</term></keywords><keywords scheme="Wicri" type="geographic" xml:lang="fr"><term>Ghana</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Now that highly active antiretroviral therapy (HAART) is being initiated on a large scale in West Africa, it remains controversial whether protease inhibitors (PIs), originally designed and tested against human immunodeficiency virus type 1 (HIV-1) subtype B, are equally effective against the non-B subtypes that are prevalent in West African countries. In this study, we investigated whether Ghanaian HIV-1 isolates, as representatives of West African isolates, are susceptible to PIs.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15983923</PMID><DateCreated><Year>2005</Year><Month>06</Month><Day>28</Day></DateCreated><DateCompleted><Year>2006</Year><Month>09</Month><Day>05</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1537-6591</ISSN><JournalIssue CitedMedium="Internet"><Volume>41</Volume><Issue>2</Issue><PubDate><Year>2005</Year><Month>Jul</Month><Day>15</Day></PubDate></JournalIssue><Title>Clinical infectious diseases : an official publication of the Infectious Diseases Society of America</Title><ISOAbbreviation>Clin. Infect. Dis.</ISOAbbreviation></Journal><ArticleTitle>HIV-1 proteases from drug-naive West African patients are differentially less susceptible to protease inhibitors.</ArticleTitle><Pagination><MedlinePgn>243-51</MedlinePgn></Pagination><Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Now that highly active antiretroviral therapy (HAART) is being initiated on a large scale in West Africa, it remains controversial whether protease inhibitors (PIs), originally designed and tested against human immunodeficiency virus type 1 (HIV-1) subtype B, are equally effective against the non-B subtypes that are prevalent in West African countries. In this study, we investigated whether Ghanaian HIV-1 isolates, as representatives of West African isolates, are susceptible to PIs.</AbstractText><AbstractText Label="METHODS" NlmCategory="METHODS">We first generated an HIV-1 protease cassette vector proviral DNA carrying a luciferase gene, which allows patient-derived HIV-1 proteases to be inserted and to be subjected to both genotypic and phenotypic assays. HIV-1 protease genes derived from 39 treatment-naive Ghanaian patients were used in this experiment as representatives of West African strains. The cloned patient-derived HIV-1 protease genes were first sequenced and then genetically compared. Phenotypic analysis was performed with Ghanaian HIV-1 protease-chimeric viruses in the presence of 6 different PIs. Structural models of HIV-1 protease homodimers were constructed by the molecular modeling software.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">Genetic analysis of cloned patient-derived HIV-1 protease genes indicated that most of the Ghanaian HIV-1 proteases are placed as subtype CRF02_AG strains, which are phylogenetically distant from subtype B strains, and that Ghanaian HIV-1 proteases do not harbor known major mutations influencing drug resistance but commonly carry 2-3 minor mutations. Phenotypic analysis performed with HIV-1 protease-recombinant viruses in the presence of 6 different PIs revealed that Ghanaian HIV-1 proteases are differentially less susceptible to the PIs. In support of this finding of differential susceptibility, structural analysis showed a significant distortion of nelfinavir, but not of amprenavir, in the Ghanaian protease pocket, suggesting nelfinavir might be less insertable into the Ghanaian protease than into the protease of subtype B.</AbstractText><AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">These findings provide implications for the combination of PIs during the introduction of HAART into West Africa.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kinomoto</LastName><ForeName>Masanobu</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Appiah-Opong</LastName><ForeName>Regina</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Brandful</LastName><ForeName>J A M</ForeName><Initials>JA</Initials></Author><Author ValidYN="Y"><LastName>Yokoyama</LastName><ForeName>Masaru</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Nii-Trebi</LastName><ForeName>Nicholas</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Ugly-Kwame</LastName><ForeName>Evelyn</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Sato</LastName><ForeName>Hironori</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Ofori-Adjei</LastName><ForeName>David</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Kurata</LastName><ForeName>Takeshi</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Barre-Sinoussi</LastName><ForeName>Françoise</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Sata</LastName><ForeName>Tetsutaro</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Tokunaga</LastName><ForeName>Kenzo</ForeName><Initials>K</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2005</Year><Month>06</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Clin Infect Dis</MedlineTA><NlmUniqueID>9203213</NlmUniqueID><ISSNLinking>1058-4838</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017320">HIV Protease Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.23.-</RegistryNumber><NameOfSubstance UI="D016333">HIV Protease</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="CommentIn"><RefSource>Clin Infect Dis. 2005 Jul 15;41(2):252-4</RefSource><PMID Version="1">15983924</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D000328" MajorTopicYN="N">Adult</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D024921" MajorTopicYN="N">Drug Resistance, Multiple, Viral</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005869" MajorTopicYN="N" Type="Geographic">Ghana</DescriptorName><QualifierName UI="Q000453" MajorTopicYN="N">epidemiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015658" MajorTopicYN="N">HIV Infections</DescriptorName><QualifierName UI="Q000821" MajorTopicYN="Y">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016333" MajorTopicYN="N">HIV Protease</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017320" MajorTopicYN="N">HIV Protease Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015497" MajorTopicYN="N">HIV-1</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2004</Year><Month>10</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2005</Year><Month>01</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>6</Month><Day>29</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>9</Month><Day>6</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>6</Month><Day>29</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15983923</ArticleId><ArticleId IdType="pii">CID35241</ArticleId><ArticleId IdType="doi">10.1086/431197</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce 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